Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Inhibitory effects of fruit powders on heterocyclic amine formation in charcoal-grilled pork: A comparative study of application methods and development of a functional barbecue sauce spray.

Food research international (Ottawa, Ont.)·2026
Same author

Unveiling mechanistic insights of inactivated Aspergillus niger spore by fishery-waste-derived chitosan via synchrotron radiation tomography.

Carbohydrate polymers·2026
Same author

Ultrasound-Assisted Deep Eutectic Solvent-Based Extraction of Polysaccharides from Okra: Optimization by Response Surface Methodology and Artificial Neural Network Modeling.

Ultrasonics sonochemistry·2025
Same author

Multifunctional chitosan-based bioactive films incorporated with Jaboticaba pomace extract for sustainable pork preservation.

International journal of biological macromolecules·2025
Same author

Bioactive Peptides from Sodium Caseinate Hydrolysate with High Oral Absorption Regulate Blood Glucose in Type 2 Diabetic Mice via Inhibition of DPP-IV and Stimulation of GLP-1.

Foods (Basel, Switzerland)·2025
Same author

Explore peptides extracted from gliadin hydrolysates suppressing BACE1 activity and restraining Aβ protein deposition.

International journal of biological macromolecules·2025

Related Experiment Video

Updated: May 26, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Proline-Based Structural Rules for Predicting Prolyl Endopeptidase Inhibitory Peptides from Food Proteins: In Vitro

Shang-Ming Huang1, Mei-Ling Li1, Ping-Jung Liu1

  • 1Department of Nutrition, China Medical University, Taichung 406040, Taiwan.

Journal of Agricultural and Food Chemistry
|May 25, 2026
PubMed
Summary

Researchers developed a novel four-rule framework to discover prolyl endopeptidase (PEP) inhibitory peptides from food proteins. This method successfully identified potent peptides, offering a new strategy for neurodegenerative disorder therapeutics.

Keywords:
MM-PBSAbioactive peptidesfood protein hydrolysatesin silico screeningmolecular dynamicsprolyl endopeptidasestructure−activity relationship

More Related Videos

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus
09:22

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus

Published on: May 31, 2022

Related Experiment Videos

Last Updated: May 26, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus
09:22

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus

Published on: May 31, 2022

Area of Science:

  • Biochemistry
  • Food Science
  • Neuroscience

Background:

  • Prolyl endopeptidase (PEP) is a key therapeutic target for neurodegenerative diseases.
  • Existing methods for discovering PEP inhibitory peptides from food proteins are limited.

Purpose of the Study:

  • To develop and validate a systematic proline-based screening framework for identifying PEP inhibitory peptides from food proteins.
  • To investigate the relationship between peptide structure and PEP inhibitory activity.

Main Methods:

  • In silico hydrolysis of 243 food proteins using a four-rule screening framework (proline presence, hydrophobic-proline motifs, consecutive proline patterns, overlap with known inhibitors).
  • Synthesis and in vitro validation of 14 candidate peptides.
  • Molecular dynamics, MM-PBSA, and quantum mechanical analyses to elucidate binding mechanisms.

Main Results:

  • The four-rule framework successfully identified 14 PEP inhibitory peptides with IC50 values ranging from 2.12 to 68.50 μM.
  • Proline presence (A1) strongly correlated with inhibitory potency (r = 0.831, p < 0.001).
  • Potency is influenced by concentrated interactions at the catalytic site, not just total contact extent, with a peptide-length confounding effect on binding energy.

Conclusions:

  • The developed proline-based screening framework offers a practical and effective strategy for prioritizing PEP inhibitory peptides from food protein hydrolysates.
  • This approach has significant implications for the discovery of novel therapeutic agents for neurodegenerative disorders.